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13 C NMR assignment of protonated carbons in d‐type porphyrins
Author(s) -
Timkovich Russell,
Bondoc Laureano L.
Publication year - 1989
Publication title -
magnetic resonance in chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.483
H-Index - 72
eISSN - 1097-458X
pISSN - 0749-1581
DOI - 10.1002/mrc.1260271107
Subject(s) - chemistry , heteronuclear molecule , protonation , heme , cytochrome , heteroatom , proton nmr , stereochemistry , hemeprotein , nitrite reductase , carbon 13 nmr , myoglobin , porphyrin , nuclear magnetic resonance spectroscopy , free base , nitrite , organic chemistry , enzyme , ring (chemistry) , ion , salt (chemistry) , nitrate
The 13 C resonances for all protonated carbons have been observed and assigned for the free base esters derived from the following natural products: heme d, the prosthetic group of the bacterial cytochrome oxidase cytochrome d; heme d 1 , the prosthetic group of the dissimilatory nitrite reductase cytochrome cd 1 ; and a stable form of sulfheme, the chemically modified prosthetic group from the degradation product of myoglobin known as sul‐fmyoglobin. These partially saturated porphyrins have in common that a heteroatom or atoms has added to a pyrrolic carbon. 13 C NMR spectra were obtained on limited amounts of naturally derived samples by proton‐detected heteronuclear correlation spectroscopy.